Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Adinarayana Marada"'
Autor:
Adinarayana Marada, Corvin Walter, Tamara Suhm, Sahana Shankar, Arpita Nandy, Tilman Brummer, Ines Dhaouadi, F.-Nora Vögtle, Chris Meisinger
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Mitochondria require an extensive proteome to maintain a variety of metabolic reactions, and changes in cellular demand depend on rapid adaptation of the mitochondrial protein composition. The TOM complex, the organellar entry gate for mitoc
Externí odkaz:
https://doaj.org/article/975ebcd39f8a4331ae240090ea03f6be
Autor:
Corvin Walter, Adinarayana Marada, Tamara Suhm, Ralf Ernsberger, Vera Muders, Cansu Kücükköse, Pablo Sánchez-Martín, Zehan Hu, Abhishek Aich, Stefan Loroch, Fiorella Andrea Solari, Daniel Poveda-Huertes, Alexandra Schwierzok, Henrike Pommerening, Stanka Matic, Jan Brix, Albert Sickmann, Claudine Kraft, Jörn Dengjel, Sven Dennerlein, Tilman Brummer, F.-Nora Vögtle, Chris Meisinger
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Mitochondrial protein import is mediated by the translocase of the outer membrane (TOM), through which nearly all precursors traverse. Here, the authors perform global in vitro kinome profiling and by this identify that DYRK1A phosphorylates TOM70 an
Externí odkaz:
https://doaj.org/article/ad335a0ad991411586d01fad9f3c40e2
Autor:
Daniel Poveda-Huertes, Asli Aras Taskin, Ines Dhaouadi, Lisa Myketin, Adinarayana Marada, Lukas Habernig, Sabrina Büttner, F-Nora Vögtle
Publikováno v:
PLoS Genetics, Vol 17, Iss 7, p e1009664 (2021)
Mitochondrial defects can cause a variety of human diseases and protective mechanisms exist to maintain mitochondrial functionality. Imbalances in mitochondrial proteostasis trigger a transcriptional program, termed mitochondrial unfolded protein res
Externí odkaz:
https://doaj.org/article/4bc527a29d51462a9590e7b42257a8e8
Autor:
Cansu Kücükköse, Sven Dennerlein, Tilman Brummer, Adinarayana Marada, A. A. Taskin, Friederike-Nora Vögtle
Publikováno v:
The FEBS Journal. 288:600-613
The mitochondrial proteome is built and maintained mainly by import of nuclear-encoded precursor proteins. Most of these precursors use N-terminal presequences as targeting signals that are removed by mitochondrial matrix proteases. The essential mit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::343bb810871a24ceb4dd66e6959ec6e5
https://doi.org/10.1111/febs.15358
https://doi.org/10.1111/febs.15358
Publikováno v:
Journal of proteomics. 252
A role for reversible phosphorylation in regulation of mitochondrial proteins has been neglected for a long time. Particularly, the import machineries that mediate influx of more than 1000 different precursor proteins into the organelle were consider
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::539fccd448d7c0273ac49729833143a5
https://pubmed.ncbi.nlm.nih.gov/34813945
https://pubmed.ncbi.nlm.nih.gov/34813945
Autor:
Lisa Myketin, Sabrina Büttner, Ines Dhaouadi, F.-Nora Vögtle, A. A. Taskin, Daniel Poveda-Huertes, Lukas Habernig, Adinarayana Marada
Publikováno v:
PLoS Genetics
PLoS Genetics, Vol 17, Iss 7, p e1009664 (2021)
PLoS Genetics, Vol 17, Iss 7, p e1009664 (2021)
Mitochondrial defects can cause a variety of human diseases and protective mechanisms exist to maintain mitochondrial functionality. Imbalances in mitochondrial proteostasis trigger a transcriptional program, termed mitochondrial unfolded protein res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef0ef649822b1879314e8b19e836faa6
http://europepmc.org/articles/PMC8282050
http://europepmc.org/articles/PMC8282050
Autor:
Arun Kumar Paripati, Thanuja Krishnamoorthy, Adinarayana Marada, Srinivasu Karri, Swati Singh, Lalitha Guruprasad, Naresh Babu V. Sepuri, Dorairajan Balasubramanian
Publikováno v:
Mitochondrion. 46:140-148
Perturbations in mitochondrial redox levels oxidize nucleotide exchanger Mge1, compromising its ability to bind to the Hsp70, while the Mxr2 enzyme reduces the oxidized Mge1. However, the effects of persistent oxidative stress on Mge1 structure and f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da220f4e2dd310b85c188a97b15ff432
https://doi.org/10.1016/j.mito.2018.04.003
https://doi.org/10.1016/j.mito.2018.04.003
Autor:
Daniel Papinski, Daniel Poveda-Huertes, Chris Meisinger, Lukas Habernig, Patrycja Mulica, F.-Nora Vögtle, Lutz Hein, Oliver Kretz, Adinarayana Marada, Sergi Tosal-Castano, Claudine Kraft, Lisa Myketin, Sabrina Büttner, Ralf Gilsbach, A. A. Taskin, Cansu Kücükköse, Stanka Matic, Mariya Licheva
Publikováno v:
Molecular Cell
Summary The mitochondrial proteome is built mainly by import of nuclear-encoded precursors, which are targeted mostly by cleavable presequences. Presequence processing upon import is essential for proteostasis and survival, but the consequences of dy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b13d427601a5a409fc704e18438bdf8d
Autor:
Srinivasu Karri, Lalitha Guruprasad, Adinarayana Marada, Yerranna Boggula, Praveen Kumar Allu, Swati Singh, Thanuja Krishnamoorthy, Naresh Babu V. Sepuri
Publikováno v:
Biochemistry. 55:7065-7072
Mge1, a yeast homologue of Escherichia coli GrpE, is an evolutionarily conserved homodimeric nucleotide exchange factor of mitochondrial Hsp70. Temperature-dependent reversible structural alteration from a dimeric to a monomeric form is critical for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::185b0251b04649b9f4ad7f93606158c8
https://doi.org/10.1021/acs.biochem.6b00232
https://doi.org/10.1021/acs.biochem.6b00232
Autor:
Adinarayana Marada, Naresh Babu V. Sepuri, Yerranna Boggula, Thanuja Krishnamoorthy, Srinivasu Karri, Praveen Kumar Allu
Publikováno v:
Molecular Biology of the Cell
Methionine sulfoxide reductases are important regulators of oxidative stress, as they reduce oxidized methionine in proteins. Mge1, a cochaperone of mtHsp70, is a physiological substrate of Mxr2 and regulates reversibly to maintain mitochondrial prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acf607475bda2742aad15a916f6329d0
http://europepmc.org/articles/PMC4310733
http://europepmc.org/articles/PMC4310733